Chemistry Letters p. 1079 - 1080 (1998)
Update date:2022-08-11
Topics:
Luo, Xuemei
Chen, Xiaohua
Song, Yongcheng
Zhu, Longgen
The [Pd(N,S-Met-a'a'H)(N,S-AcMet-aaH)] (a'a'H and aaH = amino acids) was characterized by electrospray ionization mass spectrometer(ESI-MS) and 1H NMR, in which Met-a'a'H, as ligand, coordinates to Pd(II) via thioether and terminal amino group, and AcMet-aaH, as substrate, coordinates to Pd(II) via thioether and deprotonated amide nitrogen of methionine. The Met-a'a' bond in ligand is intact, the Met-aa bond in substrate, however, is activated toward hydrolysis The difference in hydrolysis behavior between ligand and substrate may be due to a fused six-membered and five-membered ring formation via thioether, deprotonated amide nitrogen and carbonyl oxygen of methionine residue in substrate.
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